Structure of PDB 1mbt Chain A

Receptor sequence
>1mbtA (length=340) Species: 562 (Escherichia coli) [Search protein sequence]
HSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNV
LFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMP
GLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAK
ECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVT
PQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAP
NYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSED
VVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
3D structure
PDB1mbt The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R159 S229 E325
Catalytic site (residue number reindexed from 1) R157 S227 E323
Enzyme Commision number 1.3.1.98: UDP-N-acetylmuramate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FAD A I45 E48 G49 S50 N51 P111 G112 S116 I119 Q120 I122 G123 R159 I173 R214 N226 A227 G228 E325 R327 I43 E46 G47 S48 N49 P109 G110 S114 I117 Q118 I120 G121 R157 I171 R212 N224 A225 G226 E323 R325
Gene Ontology
Molecular Function
GO:0008762 UDP-N-acetylmuramate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1mbt, PDBe:1mbt, PDBj:1mbt
PDBsum1mbt
PubMed8805513
UniProtP08373|MURB_ECOLI UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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